ID DPO3B_STAES Reviewed; 377 AA.
AC Q8CQK6;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 01-MAY-2013, entry version 66.
DE RecName: Full=DNA polymerase III subunit beta;
DE EC=2.7.7.7;
GN Name=dnaN; OrderedLocusNames=SE_0002;
OS Staphylococcus epidermidis (strain ATCC 12228).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J.,
RA Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z.,
RA Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC responsible for most of the replicative synthesis in bacteria.
CC This DNA polymerase also exhibits 3' to 5' exonuclease activity.
CC The beta chain is required for initiation of replication once it
CC is clamped onto DNA, it slides freely (bidirectional and ATP-
CC independent) along duplex DNA (By similarity).
CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
CC diphosphate + DNA(n+1).
CC -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha,
CC epsilon and theta chains) that associates with a tau subunit. This
CC core dimerizes to form the POLIII' complex. PolIII' associates
CC with the gamma complex (composed of gamma, delta, delta', psi and
CC chi chains) and with the beta chain to form the complete DNA
CC polymerase III complex (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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DR EMBL; AE015929; AAO03599.1; -; Genomic_DNA.
DR RefSeq; NP_763557.1; NC_004461.1.
DR ProteinModelPortal; Q8CQK6; -.
DR STRING; 176280.SE0002; -.
DR EnsemblBacteria; AAO03599; AAO03599; SE_0002.
DR GeneID; 1056819; -.
DR KEGG; sep:SE0002; -.
DR PATRIC; 19605843; VBIStaEpi113981_0002.
DR eggNOG; COG0592; -.
DR KO; K02338; -.
DR OMA; DYNRVIP; -.
DR ProtClustDB; PRK05643; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR InterPro; IPR001001; DNA_polIII_beta.
DR InterPro; IPR022635; DNA_polIII_beta_C.
DR InterPro; IPR022637; DNA_polIII_beta_cen.
DR InterPro; IPR022634; DNA_polIII_beta_N.
DR Pfam; PF00712; DNA_pol3_beta; 1.
DR Pfam; PF02767; DNA_pol3_beta_2; 1.
DR Pfam; PF02768; DNA_pol3_beta_3; 1.
DR PIRSF; PIRSF000804; DNA_pol_III_b; 1.
DR SMART; SM00480; POL3Bc; 1.
DR TIGRFAMs; TIGR00663; dnan; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; DNA replication;
KW DNA-directed DNA polymerase; Nucleotidyltransferase; Transferase.
FT CHAIN 1 377 DNA polymerase III subunit beta.
FT /FTId=PRO_0000105469.
SQ SEQUENCE 377 AA; 42102 MW; 4188F2AFFD3BCBDD CRC64;
MMEFTIKRDY FINQLNDTLK AISPRTTLPI LTGIKIDAKE NEVILTGSDS EISIEITIPK
QVDGEEIVEI TETGSVVLPG RFFVDIIKKL PGKEVKLSTN EQFQTLITSG HSEFNLSGLD
PDQYPLLPEV SRDDAIQLSV KVLKNIIAQT NFAVSTSETR PVLTGVNWLI QDNELICTAT
DSHRLAVRKL QLEDESENKN VIIPGKALSE LNKIMSDSDE DIDIFFASNQ VLFRVGNINF
ISRLLEGHYP DTTRLFPENY EIKLGINNGD FYHAIDRASL LAREGGNNVI KLSTGNELVE
LSSTSPEIGT VKEEVNANDV EGGNLKISFN SKYMMDALKA IDNDEVEVEF FGTMKPFILK
PKDDDSVTQL ILPIRTY
//
